Mannanase Enzyme from Bacillus subtilis P2-5 with Waste Management

Optimization and Production of Alkaline Protease enzyme from Bacillus subtilis 168 isolated from food industry waste

Proteases, one among the three largest groups of industrial enzymes, accounts for about 60% of the total worldwide sale of enzymes from biological sources since they possess almost all characteristics desired for their biotechnological applications (Adinarayana et al., 2003). Among the various proteases, bacterial protease was the most significant compared with animal, fungi and plant protease....

Comparison of expression systems for the extracellular production of mannanase Man23 originated from Bacillus subtilis B23

BACKGROUND Mannanase is an enzyme that can catalyze random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans which are the key polymers in hemicellulose. It has been used in a number of different industrial applications including food, feed, pharmaceutical, pulp/paper industries, and second generation biofuel. To optimize the expression sys...

A -Mannanase from Bacillus subtilis B36: Purification, Properties, Sequencing, Gene Cloning and Expression in Escherichia coli

MANB36, a secrete endo-1,4-d-mannanase produced by Bacillus subtilis B36, was purified to homogeneity from a culture supernatant and characterized. The optimum pH value for the mannanase activity of MANB36 is 6.4 and the optimum temperature is 50 ∞C. The enzyme activity of MANB36 is remarkably thermostable at 60 ∞C and the specific activity of MANB36 is 927.84 U/mg. Metal cations (except Hg2+ a...

Isolation, Purification and Characterization of Mannanase from Bacillus subtilis MAN-511

A bacterium, MAN-511 that produced extracellular mannanase, was isolated and identified as Bacillus subtilis on the basis of 16S rDNA phylogenetic analysis. The enzyme was purified to apparent homogeneity by precipitasi ammonium sulfat 70% and Sephadex G-75 chromatography procedures. The mannanase was purified 7.6 fold and specificity of 9.3 U/mg protein. SDS-PAGE of the purified enzyme showed ...

Autolytic enzyme associated with cell walls of Bacillus subtilis.